|
Name |
Accession |
Description |
Interval |
E-value |
| RBD-FIP |
pfam09457 |
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ... |
455-495 |
1.26e-12 |
|
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.
Pssm-ID: 462805 [Multi-domain] Cd Length: 41 Bit Score: 61.97 E-value: 1.26e-12
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1092878760 455 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 495
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-480 |
5.08e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 197 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHRE----------- 265
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleaeieel 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 266 --AYGKLEREKA---TEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 340
Cdd:TIGR02168 767 eeRLEEAEEELAeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 341 LRQNRLE---FQKEREATQELIEDLRKELEHLQMYKLDCERpgRGRSASSGLGEFNARARevELEHEVKRLKQENYKLRD 417
Cdd:TIGR02168 847 IEELSEDiesLAAEIEELEELIEELESELEALLNERASLEE--ALALLRSELEELSEELR--ELESKRSELRRELEELRE 922
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878760 418 QNDDLNGQILSLSLyEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 480
Cdd:TIGR02168 923 KLAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-475 |
4.20e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 198 DITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMvKDQETTAEQALEEEARRHREAYGKLEREKAtE 277
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELLAELARLEQ-D 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 278 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQE 357
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 358 LIEDLRKELEHLQMykldcerpgrgrsassglGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLyEAKNL 437
Cdd:COG1196 380 ELEELAEELLEALR------------------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEE 440
|
250 260 270
....*....|....*....|....*....|....*...
gi 1092878760 438 FAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 475
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-370 |
1.20e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 197 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQET--TAEQALEEEARRHREAYGKLEREK 274
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEEL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 275 ATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD-EMDLYKRMMDKLRQNRLEFQKERE 353
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELE 457
|
170
....*....|....*..
gi 1092878760 354 ATQELIEDLRKELEHLQ 370
Cdd:TIGR02168 458 RLEEALEELREELEEAE 474
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
228-370 |
1.46e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 228 KQENTQLVHRVHELEEMVKD-----QETTAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTRL 302
Cdd:COG4717 87 EEEYAELQEELEELEEELEEleaelEELREELEKLEKLLQLLPLYQELEALEA-ELAELPERLEELEERLEELRELEEEL 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092878760 303 KSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 370
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
241-375 |
5.83e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.17 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 241 LEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRl 320
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE- 456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092878760 321 EDTSLRLKDEMDLYKRMMDKLRqnrlefqKEREATQELIEDLRKELEHL-QMYKLD 375
Cdd:COG2433 457 ERREIRKDREISRLDREIERLE-------RELEEERERIEELKRKLERLkELWKLE 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-469 |
7.22e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 222 DLKSKLKQENTQLVHRVHELEEMVKDqettAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTR 301
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSD----ASRKIGEIEKEIEQLEQEEEKLKE-RLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 302 LKSQTEKLDEERQRMSDRLEDTSLRLKDE-MDLYKRMMDKLRQNRLEFQKE-REATQEL------IEDLRKELEHLQMYK 373
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARlREIEQKLnrltleKEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 374 LDCERpgrgRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSlyeaKNLFAAQTKAQSLAAEIDT 453
Cdd:TIGR02169 843 IDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE----AQLRELERKIEELEAQIEK 914
|
250
....*....|....*.
gi 1092878760 454 AsrDELMEALKEQEEI 469
Cdd:TIGR02169 915 K--RKRLSELKAKLEA 928
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-474 |
7.61e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 201 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKD-----QETTAEQA-LEEEARRHREAYGKLEREK 274
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelYALANEISrLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 275 atevELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREA 354
Cdd:TIGR02168 319 ----EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 355 TQELIEDLRKELEhlqmykldcerpgrgrsassglgefNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYE- 433
Cdd:TIGR02168 391 LELQIASLNNEIE-------------------------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEl 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1092878760 434 -------AKNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINFRLR 474
Cdd:TIGR02168 446 eeeleelQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLD 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
190-365 |
9.75e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 190 DSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ------ALEEEARRH 263
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlesrlgDLKKERDEL 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 264 REAYGKLER----------EKATEVELLNARVQQLEEENTELRTTVTRLKSQT------EKLDEERQRMSDR---LEDTS 324
Cdd:TIGR02169 895 EAQLRELERkieeleaqieKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEiraLEPVN 974
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092878760 325 LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE 365
Cdd:TIGR02169 975 MLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
200-367 |
1.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 200 TEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAE-QALEEEARRHREAYGKLEREKAT-- 276
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 277 ----EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEM--DLYKR----MMDKLRQN-R 345
Cdd:COG4913 689 aleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraLLEERfaaaLGDAVERElR 768
|
170 180
....*....|....*....|..
gi 1092878760 346 LEFQKEREATQELIEDLRKELE 367
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELE 790
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
198-471 |
1.59e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 198 DITEKVSFLEKKVTELENDSLTNGDLKSKLKqentQLVHRVHELEEMVKDQETTaeQALEEEARRHREAYGKLEREKAT- 276
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA--KAKKEELERLKKRLTGLTPEKLEk 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 277 EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDE--ERQRMSDRLEDTSLRLKDEMDlYKRMMDKLRQNRLEFQKEREA 354
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEH-RKELLEEYTAELKRIEKELKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 355 TQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEFNARAREVELEhEVKRLKQENYKLRDQNDDLNGQILSLsLYEA 434
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL 548
|
250 260 270
....*....|....*....|....*....|....*..
gi 1092878760 435 KNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINF 471
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEE-ELAELLKELEELGF 584
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
246-370 |
2.06e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 246 KDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSL 325
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1092878760 326 RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 370
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
240-480 |
3.04e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 240 ELEEMVKDQETTAEQalEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 319
Cdd:TIGR02168 233 RLEELREELEELQEE--LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 320 ---LEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCER----------PGRGRSAS 386
Cdd:TIGR02168 311 lanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqleTLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 387 SGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQ 466
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250
....*....|....
gi 1092878760 467 EEINFRLRQYMDKI 480
Cdd:TIGR02168 471 EEAEQALDAAEREL 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
228-370 |
3.67e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 228 KQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTE 307
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092878760 308 KLD------EERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 370
Cdd:TIGR02169 393 KLEklkreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
226-475 |
6.20e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 226 KLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKAT---EVELLNARVQQLEEENTELRTTVTRL 302
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlerSIAEKERELEDAEERLAKLEAEIDKL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 303 KSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcERPGRG 382
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRD----KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK------REINEL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 383 RSASSGLGEFNARARE--VELEHEVKRLKQENYKLRDQNDDLngqilslslyeAKNLFAAQTKAQSLAAEIDTAsRDELM 460
Cdd:TIGR02169 405 KRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEEKEDK-----------ALEIKKQEWKLEQLAADLSKY-EQELY 472
|
250
....*....|....*
gi 1092878760 461 EALKEQEEINFRLRQ 475
Cdd:TIGR02169 473 DLKEEYDRVEKELSK 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
189-370 |
7.52e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 189 RDSIDSCDNDITEKVSFLEKKVTELENDSLTN----GDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEE------ 258
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALeaelAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspe 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 259 ---EARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQrmsdrledtslRLKDEMDLYK 335
Cdd:COG4942 130 dflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-----------ALEALKAERQ 198
|
170 180 190
....*....|....*....|....*....|....*
gi 1092878760 336 RMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 370
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-468 |
1.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 252 AEQAL------EEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTS- 324
Cdd:COG1196 209 AEKAEryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 325 ---------LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcerpgrgrsASSGLGEFNAR 395
Cdd:COG1196 289 eeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--------------EELEEAEEELE 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878760 396 AREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEE 468
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
209-371 |
1.74e-05 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 46.56 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 209 KVTELENDSLtNGDLKSkLKQENTQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREaygKLEREKATEVELLNA 283
Cdd:pfam04849 97 SVLTERNEAL-EEQLGS-AREEILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 284 RVQQLEEENTELRTTVTRLKSQTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQEL 358
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEE 239
|
170
....*....|...
gi 1092878760 359 IEDLRKELEHLQM 371
Cdd:pfam04849 240 ITSLLAQIVDLQH 252
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
224-418 |
8.09e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 224 KSKLKQENTQ--LVHRVHELEEMVKDQETTAE---QALEEEARRHREAYGKLEREKATEVEllnaRVQQLEEENTELRTT 298
Cdd:pfam17380 403 KVKILEEERQrkIQQQKVEMEQIRAEQEEARQrevRRLEEERAREMERVRLEEQERQQQVE----RLRQQEEERKRKKLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 299 VTRLKSQTEKLDEERQRMsdrledtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQELI--EDLRKELEHLQMYKLDC 376
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKI----------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEM 548
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092878760 377 ERPGRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQ 418
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-470 |
8.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 254 QALEEEARRHREAYGKLEREKATEVELLNA--RVQQLEEENTELRTTVTRLksqtEKLDEERQRM---SDRLEdtslRLK 328
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREI----AELEAELERLdasSDDLA----ALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 329 DEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASsglgEFNARAREVELEHEVKRL 408
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----LLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092878760 409 KQEnykLRDQNDDLNGQILSLS--LYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEIN 470
Cdd:COG4913 768 REN---LEERIDALRARLNRAEeeLERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
224-493 |
1.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 224 KSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLK 303
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 304 SQTEKLDEERQRMSDRLEDTSLRLKDEMDLyKRMMDKLRQNRLEFQKEREATQELIEDLRKELEH----LQMYKLDCERP 379
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkaAEALKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 380 GRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDEL 459
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
250 260 270
....*....|....*....|....*....|....
gi 1092878760 460 MEALKEQEEinfRLRQYMDKIILAILDHNPSILE 493
Cdd:PTZ00121 1782 EEELDEEDE---KRRMEVDKKIKDIFDNFANIIE 1812
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
253-433 |
1.24e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 253 EQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSD-------------- 318
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreeleklekllql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 319 -----RLEDTSLRLKDEMDLYKRMMDKLRQnRLEFQKEREATQELIEDLRKELEHLQMyKLDCERPGRGRSASSGLGEfn 393
Cdd:COG4717 128 lplyqELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLE-QLSLATEEELQDLAEELEE-- 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092878760 394 ARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYE 433
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
222-449 |
1.53e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 222 DLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEArrhreaygKLEREKATEVELLNARVQQLEEENTELRTTVTR 301
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA--------ALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 302 LKSQTEKLDEERQRMSDRL-----------------EDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRK 364
Cdd:COG4942 92 IAELRAELEAQKEELAELLralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 365 ELEHLQMYKLDCERpgRGRSASSGLGEfnARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNlfAAQTKA 444
Cdd:COG4942 172 ERAELEALLAELEE--ERAALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA--AERTPA 245
|
....*
gi 1092878760 445 QSLAA 449
Cdd:COG4942 246 AGFAA 250
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
201-370 |
1.62e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 201 EKVSfLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ-----------ALEEEARRHREAYGK 269
Cdd:pfam01576 125 EKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSlsklknkheamISDLEERLKKEEKGR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 270 LEREKATevellnarvQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLR------- 342
Cdd:pfam01576 204 QELEKAK---------RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIReleaqis 274
|
170 180 190
....*....|....*....|....*....|.
gi 1092878760 343 --QNRLEFQK-EREATQELIEDLRKELEHLQ 370
Cdd:pfam01576 275 elQEDLESERaARNKAEKQRRDLGEELEALK 305
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-411 |
1.69e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 237 RVHELEEMVKDQETTAEQALEEEARRHREAYGKLEReKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRM 316
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 317 SDRLEDTSLRLKDEMdlyKRMMDKLRQNRLEFQKEREATQELIEDL-------RKELEHLQmyKLDCERPGRGRSASSGL 389
Cdd:COG4913 329 EAQIRGNGGDRLEQL---EREIERLERELEERERRRARLEALLAALglplpasAEEFAALR--AEAAALLEALEEELEAL 403
|
170 180
....*....|....*....|....
gi 1092878760 390 GE--FNARAREVELEHEVKRLKQE 411
Cdd:COG4913 404 EEalAEAEAALRDLRRELRELEAE 427
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
258-474 |
1.73e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 258 EEARRHREAYGKLEREKATEVELLNARVQQLEEEN-----TELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL----- 327
Cdd:PRK02224 169 ERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLeehee 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 328 -KDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLqmykldcERPGRGRSASSGLGEFNARA---REVELEH 403
Cdd:PRK02224 249 rREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-------EEERDDLLAEAGLDDADAEAveaRREELED 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092878760 404 EVKRLKQENYKLRDQNDDLNGQILSLsLYEAKNLFAAQTKAQSLAAEIDT---ASRDELMEALKEQEEINFRLR 474
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESL-REDADDLEERAEELREEAAELESeleEAREAVEDRREEIEELEEEIE 394
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
228-367 |
2.38e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 228 KQENTQLVHRVHELEEMVKDQETTAEQALEE-EARRHreaYGKLEREKATEVELLNARVQQLEEENTELRttvtrlKSQT 306
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQElEAARK---VKILEEERQRKIQQQKVEMEQIRAEQEEAR------QREV 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092878760 307 EKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELE 367
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
227-378 |
2.92e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 227 LKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQT 306
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARE 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092878760 307 EKLDEERQRMSDRLEdtslrlkdemdlykrmmdklrqnRLEFQKEREATQELIEDLRKELEH--LQMYKLDCER 378
Cdd:PRK12705 119 LELEELEKQLDNELY-----------------------RVAGLTPEQARKLLLKLLDAELEEekAQRVKKIEEE 169
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
204-368 |
4.07e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 204 SFLEKKVTELENDSltngdlKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNA 283
Cdd:PRK12704 27 KIAEAKIKEAEEEA------KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 284 RVQQLEEENTELRTTVTRLKSQTEKLDEERQRmsdrledtslrlkdemdlYKRMMDKLRQnRLE----FQKErEATQELI 359
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEE------------------LEELIEEQLQ-ELErisgLTAE-EAKEILL 160
|
....*....
gi 1092878760 360 EDLRKELEH 368
Cdd:PRK12704 161 EKVEEEARH 169
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-327 |
6.74e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 198 DITEKVSFLEKKVTELENDSltnGDLKSKLKQENTQL--VHRVHELEEMVKDQETTAE--QALEEEARRHREAYGKLERE 273
Cdd:COG1579 49 AAKTELEDLEKEIKRLELEI---EEVEARIKKYEEQLgnVRNNKEYEALQKEIESLKRriSDLEDEILELMERIEELEEE 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1092878760 274 KATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL 327
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
238-466 |
8.07e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 238 VHELEEMVKDQETTAEQALEEEARRHREAYGKLERE-KATEVEllnaRVQQLEEENTELRTTVTR---LKSQTEKLDEER 313
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEeKAREVE----RRRKLEEAEKARQAEMDRqaaIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 314 QRMSDRLedtslRLKDEmdlyKRMMDKLRQNRL--EFQKERE------ATQELIEDLRKELEHLQMYKLDCERPGRGRSA 385
Cdd:pfam17380 347 ERELERI-----RQEER----KRELERIRQEEIamEISRMRElerlqmERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 386 SSGLGEF------NARAREV-----ELEHEVKRLKQENY-------KLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSL 447
Cdd:pfam17380 418 QKVEMEQiraeqeEARQREVrrleeERAREMERVRLEEQerqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL 497
|
250
....*....|....*....
gi 1092878760 448 AAEIDTASRDELMEALKEQ 466
Cdd:pfam17380 498 EKELEERKQAMIEEERKRK 516
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
146-480 |
1.02e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 146 LEARLKNLKANSPNRKISSTAFGRQLMHSSNFSSSNGSTEDLFRDSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKS 225
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 226 KLKQENTQL-VHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKS 304
Cdd:pfam02463 768 ELSLKEKELaEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 305 QTEKLDEERQRmsDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEhlqmykldcerpgrgrs 384
Cdd:pfam02463 848 LEKLAEEELER--LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK----------------- 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 385 assglgEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEAL- 463
Cdd:pfam02463 909 ------LNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEe 982
|
330
....*....|....*....
gi 1092878760 464 --KEQEEINFRLRQYMDKI 480
Cdd:pfam02463 983 feEKEERYNKDELEKERLE 1001
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
199-369 |
1.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 199 ITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQA-----LEEEARRHREAYGKLERE 273
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAeeyikLSEFYEEYLDELREIEKR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 274 KAT-------------EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMsDRLEDTSLRLKD-EMDLYKRMMD 339
Cdd:PRK03918 316 LSRleeeingieerikELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-EELERLKKRLTGlTPEKLEKELE 394
|
170 180 190
....*....|....*....|....*....|
gi 1092878760 340 KLRQNRLEFQKEREATQELIEDLRKELEHL 369
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
206-319 |
1.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 206 LEKKVTELENDSLTN-GDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREKATEVELLNAR 284
Cdd:COG4913 321 LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAA-LGLPLPASAEEFAALRAEAAALLEALEEE 399
|
90 100 110
....*....|....*....|....*....|....*
gi 1092878760 285 VQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 319
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
212-371 |
1.78e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 40.82 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 212 ELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKA------------TEVE 279
Cdd:COG5244 394 EDNKDVTLILKILHPILETTVPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKLIGKEEISKQdnrlflypscdiTLSS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 280 LLNARVQ-------QLEEENTELRTTVTRLKSQTEKLDE---ERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRL--E 347
Cdd:COG5244 474 ILTILFSdklevffQGIESLLENITIFPEQPSQQTSDSEnikENSLLSDRLNEENIRLKEVLVQKENMLTEETKIKIiiG 553
|
170 180
....*....|....*....|....
gi 1092878760 348 FQKEREATQELIEDLRKELEHLQM 371
Cdd:COG5244 554 RDLERKTLEENIKTLKVELNNKNN 577
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
206-365 |
3.26e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 206 LEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEqALEEEARRHREAYGKLERE---KATEVELLN 282
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK-VLSRSINKIKQNLEQKQKElksKEKELKKLN 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 283 ARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLED------------TSLRLKDEMDLYKRMMDKLRQNRLEFQK 350
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
170
....*....|....*
gi 1092878760 351 EREATQELIEDLRKE 365
Cdd:TIGR04523 583 KQEEKQELIDQKEKE 597
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
272-475 |
3.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 272 REKATEVelLNARVQQLEEENTELRTTVTRlkSQTEKLDEERQRMSDRLEDTSLRLKD------------EMDLYKRMMD 339
Cdd:COG3206 147 PELAAAV--ANALAEAYLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEfrqknglvdlseEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 340 KLRQNRLEFQKEREATQELIEDLRKELEhlqmykldcERPGRGRSASSGLGEFNARAREVELEHEVKRLKQ---ENY--- 413
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLG---------SGPDALPELLQSPVIQQLRAQLAELEAELAELSArytPNHpdv 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092878760 414 -KLRDQNDDLNGQILSLSlyeAKNLFAAQTKAQSLAAEIDT--ASRDELMEALKEQEEINFRLRQ 475
Cdd:COG3206 294 iALRAQIAALRAQLQQEA---QRILASLEAELEALQAREASlqAQLAQLEARLAELPELEAELRR 355
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
271-471 |
3.64e-03 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 39.59 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 271 EREKATEVELLNARVQQLEEENTElrtTVTRLKSQTEKLDEERQRMSDRLE-----------DTSLRLKDEMDLYKRMMD 339
Cdd:NF033928 100 KRGDLTEEELSELPPIPLSSDDKE---IVKELKEILEDLKNDIKDYQQKADdvkkelddfenDLREELLPQLKLKKKLYD 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 340 KLRQNrlefqKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEF-----------NARAREVELEHEVKRL 408
Cdd:NF033928 177 DNLGS-----DSIEELREKIDQLEKEIEQLNKEYDDYVKLSFTGLAGGPIGLAitggifgskaeKIRKEKNALIQEIDEL 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092878760 409 KQenyKLRDQN------DDLNGQILSLSLYEAKNLFAAQTKA---QSLAAEIDtASRDELMEALKEQEEINF 471
Cdd:NF033928 252 QE---QLKKKNallgslERLQTSLDDILTRMEDALPALKKLKgvwQSLLTDID-SSINALKEIDDADSLRLF 319
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
196-369 |
3.67e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 196 DNDITEKVSFLEKKVTELENDSltngdlkSKLKQENTQLVHRVHELEEMVKDQETTAE--QALEEEARRHREAYGKLERE 273
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEI-------ERYEEQREQARETRDEADEVLEEHEERREelETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 274 KAT---EVELLNARVQQLEEENTELRTTV-------TRLKSQTEKLDEERQRMSDRLEDTSL----------RLKDEMDL 333
Cdd:PRK02224 274 REElaeEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVaaqahneeaeSLREDADD 353
|
170 180 190
....*....|....*....|....*....|....*.
gi 1092878760 334 YKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHL 369
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
229-483 |
3.86e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 39.58 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 229 QENTQLVHRVHELEEMVKDQETTAEQALEEEARRhreaygklerekaTEVELLNARVQQLEEENT----ELRTTVTRLKS 304
Cdd:PRK10361 26 QHAQQKAEQLAEREEMVAELSAAKQQITQSEHWR-------------AECELLNNEVRSLQSINTsleaDLREVTTRMEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 305 -QTEKLDEERQRMSdrledTSLRLKDEMD-LYKRMMDKlrQNRLEFQKEREATQELIEDLRKELEhlqmykldcerpGRG 382
Cdd:PRK10361 93 aQQHADDKIRQMIN-----SEQRLSEQFEnLANRIFEH--SNRRVDEQNRQSLNSLLSPLREQLD------------GFR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 383 RSASSGLGEfNARAREVeLEHEVKRLKQENYKLRDQNDDLN-------------GQILSLSLYEAKNLFAAQTKAQSLAA 449
Cdd:PRK10361 154 RQVQDSFGK-EAQERHT-LAHEIRNLQQLNAQMAQEAINLTralkgdnktqgnwGEVVLTRVLEASGLREGYEYETQVSI 231
|
250 260 270
....*....|....*....|....*....|....
gi 1092878760 450 EIDTASRdelmealkEQEEINFRLRQYMDKIILA 483
Cdd:PRK10361 232 ENDARSR--------MQPDVIVRLPQGKDVVIDA 257
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
233-365 |
4.48e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 39.73 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 233 QLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLerekATEVELLNARVQQLEEENTELRTTVTRLK-----SQTE 307
Cdd:pfam07111 506 QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASV----GQQLEVARQGQQESTEEAASLRQELTQQQeiygqALQE 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092878760 308 KLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQE---LIEDLRKE 365
Cdd:pfam07111 582 KVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQElrrLQDEARKE 642
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
254-370 |
4.89e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 254 QALEEEARRHREAYGKLEREkatevellnarVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD---- 329
Cdd:COG1579 13 QELDSELDRLEHRLKELPAE-----------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeq 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092878760 330 ---------------EMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 370
Cdd:COG1579 82 lgnvrnnkeyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
237-422 |
5.11e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 237 RVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRM 316
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 317 SDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcerpgRGRSAssgLGEFNARA 396
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE----------REIEA---LGPVNLLA 786
|
170 180
....*....|....*....|....*.
gi 1092878760 397 REvELEHEVKRLKqenyKLRDQNDDL 422
Cdd:COG1196 787 IE-EYEELEERYD----FLSEQREDL 807
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
242-430 |
5.29e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 242 EEMVKDQETTAEQAL---EEEARRHREAY-------GKLEREKA--TEVELLN---------ARVQQLEEENTELRTTVT 300
Cdd:COG3096 450 EQQATEEVLELEQKLsvaDAARRQFEKAYelvckiaGEVERSQAwqTARELLRryrsqqalaQRLQQLRAQLAELEQRLR 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 301 RLKSQTEKLDEERQRMS------DRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE--------- 365
Cdd:COG3096 530 QQQNAERLLEEFCQRIGqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqd 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092878760 366 -LEHLqmykldCERPGRGRSASSGLGEFnaRAREVELEHEVKRLKQEnykLRDQNDDLNGQILSLS 430
Cdd:COG3096 610 aLERL------REQSGEALADSQEVTAA--MQQLLEREREATVERDE---LAARKQALESQIERLS 664
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
201-332 |
5.57e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 37.28 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 201 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALeeearrhreaygklerEKATEVEL 280
Cdd:pfam12718 14 ERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESE----------------KLKTNNEN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092878760 281 LNARVQQLEEE----NTELRTTVTRLKsQTEKLDEERQRMSDRLEDTSLRLKDEMD 332
Cdd:pfam12718 78 LTRKIQLLEEEleesDKRLKETTEKLR-ETDVKAEHLERKVQALEQERDEWEKKYE 132
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
241-423 |
6.33e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 241 LEEMVKDQETTAEQAlEEEARRHREAYG--KLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSD 318
Cdd:COG3206 180 LEEQLPELRKELEEA-EAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 319 RLEDTSL-RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEhlqmykldcERPGRGRSASSGLGEfNARAR 397
Cdd:COG3206 259 LLQSPVIqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---------QEAQRILASLEAELE-ALQAR 328
|
170 180
....*....|....*....|....*.
gi 1092878760 398 EVELEHEVKRLKQENYKLRDQNDDLN 423
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELR 354
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
254-370 |
6.46e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.50 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 254 QALEEEARRHREAYGKLEREKATE-----VELLNARVQQLEEENTELRTTVTRLKSQTEK----LDEERQRMSDRLEDTS 324
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKdqtaLETLEKALKDLLTDEG 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1092878760 325 LRL-KDEMDLYKRMMDKLRQN-RLEFQKEREATQELIEDLRKELEHLQ 370
Cdd:cd22656 174 GAIaRKEIKDLQKELEKLNEEyAAKLKAKIDELKALIADDEAKLAAAL 221
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
236-332 |
6.50e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 37.21 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 236 HRVHELEEMVKDQETTAEQALEEEA--RRHREAYGKLEREKATEVELLNARVQQLEEENTELRTT-VTRLKSQTEKLDEE 312
Cdd:pfam09744 47 EHNVELEELREDNEQLETQYEREKAlrKRAEEELEEIEDQWEQETKDLLSQVESLEEENRRLEADhVSRLEEKEAELKKE 126
|
90 100
....*....|....*....|
gi 1092878760 313 RQRMSDRLEDTSLRLKDEMD 332
Cdd:pfam09744 127 YSKLHERETEVLRKLKEVVD 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
228-431 |
6.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 228 KQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYgkLEREKATEVELLNARVQQLEEENtELRTTVTRLKSQTE 307
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 308 KLDEERQRMSDRLEDTSLRLKDEmdlykrmmdklrqnrlEFQKEREATQELIEDLRKElehlqmykldcerpgrgrsass 387
Cdd:COG4717 413 ELLGELEELLEALDEEELEEELE----------------ELEEELEELEEELEELREE---------------------- 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1092878760 388 gLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSL 431
Cdd:COG4717 455 -LAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
272-475 |
7.59e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.01 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 272 REKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYkrmmdklrqNRLEFQKE 351
Cdd:PRK10246 415 LAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL---------ADVKTICE 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 352 REATQELIEDLRKELEHLQMYKL--DCERPGRGRSASSGLGEfnARAREVELEHEVKRLKQENYKLRDQNDDLNGQIL-- 427
Cdd:PRK10246 486 QEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQALEPGV--NQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQrd 563
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1092878760 428 ---SLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 475
Cdd:PRK10246 564 eseAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRL 614
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-364 |
8.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 201 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATevel 280
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR---- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 281 LNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTslrlkdemdlykrmMDKLRQNRLEFQKEREATQELIE 360
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA--------------LAEAEAALRDLRRELRELEAEIA 429
|
....
gi 1092878760 361 DLRK 364
Cdd:COG4913 430 SLER 433
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
235-346 |
9.39e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 36.46 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878760 235 VHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLERE---KATEVELLnarvQQLEEENTELRTTVTRLKSQTEKLDE 311
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvlHAEDIKAL----QALREELNELKAEIAELKAEAESAKA 85
|
90 100 110
....*....|....*....|....*....|....*.
gi 1092878760 312 ERQRMSDRLEDTSLRLKDEMDLYKRMMDKLR-QNRL 346
Cdd:pfam07926 86 ELEESEESWEEQKKELEKELSELEKRIEDLNeQNKL 121
|
|
| |
